Evidence map›Paper›PMID 32316569›Full record

ArticleBiomolecules2020

Physicochemical Characterisation of KEIF-The Intrinsically Disordered N-Terminal Region of Magnesium Transporter A.

Stéphanie Jephthah, Linda K Månsson, Domagoj Belić, Jens Preben Morth, Marie Skepö

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 35% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. P-type ATPase magnesium transporter MgtA acts as a dimer.Nature structural & molecular biology · 2025
    Article
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  3. Article
  4. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Stéphanie JephthahDivision of Theoretical Chemistry, Department of Chemistry, Lund University, Naturvetarvägen 14, 221 00 Lund, Sweden.ORCID 0000-0003-4287-506X
Linda K MånssonDivision of Theoretical Chemistry, Department of Chemistry, Lund University, Naturvetarvägen 14, 221 00 Lund, Sweden.
Domagoj BelićDivision of Physical Chemistry, Department of Chemistry, Lund University, Naturvetarvägen 14, 221 00 Lund, Sweden.
Jens Preben MorthEnzyme and Protein Chemistry, Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, Technical University of Denmark, Søltofts Plads, 2800 Kgs. Lyngby, Denmark.
Marie SkepöDivision of Theoretical Chemistry, Department of Chemistry, Lund University, Naturvetarvägen 14, 221 00 Lund, Sweden.ORCID 0000-0002-8639-9993
Lund University · SETechnical University of Denmark · DK

Funding

NordForsk 81912Science Faculty project grant program for research on neutrons and synchrotron light (Lund University Strategic 529 funds for MAX-IV and European Spallation Source) -
6 · The paper itself

Abstract

Magnesium transporter A (MgtA) is an active transporter responsible for importing magnesium ions into the cytoplasm of prokaryotic cells. This study focuses on the peptide corresponding to the intrinsically disordered N-terminal region of MgtA, referred to as KEIF. Primary-structure and bioinformatic analyses were performed, followed by studies of the undisturbed single chain using a combination of techniques including small-angle X-ray scattering, circular dichroism spectroscopy, and atomistic molecular-dynamics simulations. Moreover, interactions with large unilamellar vesicles were investigated by using dynamic light scattering, laser Doppler velocimetry, cryogenic transmission electron microscopy, and circular dichroism spectroscopy. KEIF was confirmed to be intrinsically disordered in aqueous solution, although extended and containing little β -structure and possibly PPII structure. An increase of helical content was observed in organic solvent, and a similar effect was also seen in aqueous solution containing anionic vesicles. Interactions of cationic KEIF with anionic vesicles led to the hypothesis that KEIF adsorbs to the vesicle surface through electrostatic and entropic driving forces. Considering this, there is a possibility that the biological role of KEIF is to anchor MgtA in the cell membrane, although further investigation is needed to confirm this hypothesis.

Indexed as

Chemical PhenomenaAdenosine TriphosphatasesAmino Acid MotifsAmino Acid SequenceCircular DichroismEscherichia coliEscherichia coli ProteinsIntrinsically Disordered ProteinsLipidsMembrane Transport ProteinsMolecular Dynamics SimulationParticle SizeProbabilityProtein Structure, SecondaryScattering, Small AngleUnilamellar LiposomesAdenosine TriphosphatasesEscherichia coli ProteinsIntrinsically Disordered ProteinsLipidsMembrane Transport ProteinsMgtA protein, E coliUnilamellar Liposomescircular dichroism spectroscopycryogenic transmission electron microscopyintrinsically disordered proteinsmagnesium transportermembrane proteinsmolecular-dynamics simulationsprotein–vesicle interactionssecondary structure.small-angle X-ray scattering

Identifiers

PMID32316569
PMCPMC7226168
OpenAlexW3017113381

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.